Structural and Dynamic Views of GM1 Ganglioside

Overview

Journal Glycoconj J

Publisher Springer

Specialties Biochemistry
Endocrinology

Date 2015 May 2

PMID 25931034

Citations 11

Authors

Maho Yagi-Utsumi

Koichi Kato

Affiliations

Soon will be listed here.

Abstract

The ganglioside GM1 mediates various physiological and pathological processes mainly through the formation of GM1 clusters on cell surfaces. Therefore, detailed characterization of conformational properties of the glycan moiety of GM1 and the structures and interactions of this glycosphingolipid in membrane environments is necessary for better understanding of the clustering-coupled functional promotion. Nuclear magnetic resonance (NMR) spectroscopy has provided conformational information of GM1 in solution as well as in membrane-like environments. Recently, sophisticated paramagnetism-assisted NMR approaches combined with molecular dynamics simulations have enabled the quantitative exploration of conformational spaces of a series of gangliosides, including GM1, taking into account their minor conformations. NMR techniques have also been successfully applied to investigations of the dynamic interactions of GM1 clusters with amyloidogenic proteins such as amyloid β and α-synuclein associated with neurodegenerative disorders. Further integration of experimental and computational approaches will open up new possibilities to provide structural views of the more complicated heterogeneous systems exemplified by microdomains involving GM1.

Citing Articles

Prevention of amyloid β fibril deposition on the synaptic membrane in the precuneus by ganglioside nanocluster-targeting inhibitors.

Miyamoto E, Hayashi H, Murayama S, Yanagisawa K, Sato T, Matsubara T RSC Chem Biol. 2024; 5(5):459-466.

PMID: 38725912 PMC: 11078214. DOI: 10.1039/d4cb00038b.

GM1 structural requirements to mediate neuronal functions.

Fazzari M, Lunghi G, Di Biase E, Maggioni M, Carsana E, Cioccarelli L Glycoconj J. 2023; 40(6):655-668.

PMID: 38100017 DOI: 10.1007/s10719-023-10141-8.

AB Toxins as High-Affinity Ligands for Cell Targeting in Cancer Therapy.

Marquez-Lopez A, Fanarraga M Int J Mol Sci. 2023; 24(13).

PMID: 37446406 PMC: 10343017. DOI: 10.3390/ijms241311227.

Structural Analysis of Oligosaccharides and Glycoconjugates Using NMR.

Yamaguchi Y, Yamaguchi T, Kato K Adv Neurobiol. 2022; 29:163-184.

PMID: 36255675 DOI: 10.1007/978-3-031-12390-0_6.

Conformational Variability of Amyloid-β and the Morphological Diversity of Its Aggregates.

Yagi-Utsumi M, Kato K Molecules. 2022; 27(15).

PMID: 35897966 PMC: 9369837. DOI: 10.3390/molecules27154787.

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